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Lists articles about biochemistry. "Modulation of the interaction between the two halves of troponin C by the other troponin subunits," by C.-L.A. Wang and J. Gergely; "Sequence determinants of cytosolic N-terminal protein processing," by C. Flinta, B. Persson, H. Jornvall and G. von Heijne; "Effect of benzoate on the metabolism of fructose 2,6-biphosphate in yeast," by J. Francois, E. van Schaftingen and H.-G. Hers; "Isolation and properties of porcine cholesterol acyltransferase," G. Knipping; Others.

A protein is usually classified into one of the following four structural classes: all α, all β, (a + B) and α/β. In this paper, based on the maximum correlation-coefficient principle, a new formulation is proposed for predicting the structural class of a protein according to its amino acid composition. Calculations have been made for a development set of proteins from which the amino acid compositions for the standard structural classes were derived, and an independent set of proteins which are outside the development set. The former can test the self consistency of a method and the latter can test its extrapolating effectiveness. In both cases, the results showed that the new method gave a considerably higher rate of correct prediction than any of the previous methods, implying that a significant improvement has been achieved by implementing the maximum-correlation-coefficient principle in the new method. [ABSTRACT FROM AUTHOR]

A theory is proposed to explain the physical bases of the ionic control of the activity of an enzyme system, located on a plant cell surface, and probably involved in cell-wall synthesis and extension. The model, which is based on various previously published experimental results, involves several assumptions: a cell-wall pectin methyl esterase de-esterifies pectins and thus creates the fixed negative charges of the cell wall; various enzymes incorporate uncharged carbohydrates in cell-wall material; cell-wall extension implies the sliding of cellulose microfibrils; the enzymes responsible for carbohydrate incorporation are activated by protons in the pH range 4-8 and have very similar pH dependencies: the cell-wall pectin methyl esterase is inhibited by protons in the same pH range. The mathematical derivation of this model, written in the form of a hypercycle, indicates that it is equivalent to a set of two antagonistic enzyme reactions: an enzyme reaction conditioned by pectin methyl esterase which results in the increase of fixed charge density of the cell wall; a number of 'growth enzymes', which produce extension and building up of the cell wall and therefore a decrease of charge density. The mathematical study of this model shows it may display a very high co-operativity of its response to slight changes of pH. This co-operativity means that the cell wall charge density may dramatically increase or decrease, within a very narrow pH range. The steep response of this system appears to be the direct consequence of different pH sensitivities of pectin methyl esterase and of the other cell-wall enzymes involved in cell growth. Calcium, which tightly binds to the cell wall, may diminish or even suppress this abrupt charge transition. This model suggests a novel theory of the ionic control of cell-wall expansion. The very basis of this theory is the existence of an electrostatic potential difference, Δψ, between the inside and the outside of the cell wall. When this Δψ value is large, the local proton concentration is high. Therefore the enzymes involved in cell wall extension and building up are active, but pectin methyl esterase is not. Therefore, the cell wall extends and the charge density decreases. The Δψ value then declines, as well as the local proton concentration. Under these conditions, the pectin methyl esterase becomes activated, whereas the 'growth enzymes' are not. This activation of pectin methyl esterase restores the initial, or an even higher, clectrostatic potential difference, which in turn results in a decrease of local pH. In the following papers the basic ideas of this model are subjected to experimental control. [ABSTRACT FROM AUTHOR]

This paper considers how apolipoprotein CII from human plasma lipoproteins and T1 and T2 proteins from egg yolk Iipoproteins stimulate the activity oflipoprotein lipase. These activator proteins stabilized the enzyme much more effectively than a thousandfold higher concentration of albumin did, indicating a direct interaction with the enzyme. The effects of the activators were seen also at 1 M NaCl. Thus, forces other than electrostatic are implicated. Centrifugation experiments showed that 125I-labeled lipase bound equally well to the emulsion droplets in the absence of activator protein as in its presence. This was true even under conditions when the activator caused a severalfold increase in the rate of hydrolysis. Thus, the activator makes enzyme at the interface more effective in hydrolysis. By optimizing the conditions it was possible to obtain almost as high rates of triglyceride hydrolysis in the absence as in the presence of activator. Thus, the main effect of the activator protein is probably not on a rate-limiting chemical step. Under most conditions, the rate of hydrolysis was much below optimal and activator increased it. This was always the case with phosphatidyl-choline/triglyceride emulsions, where the activator enhanced hydrolysis of both lipids. Other experiments showed that the activator enhanced triglyceride hydrolysis in the absence of phospholipids and phospholipid hydrolysis in the absence of triglycerides. It is suggested that interaction with activator orientates the enzyme and/or the lipid substrate for effective hydrolysis at the surface of lipoproteins/model substrates. [ABSTRACT FROM AUTHOR]

We have further characterized the polynucleotide ligase purified from cultures of the human heteroploid line EUE [Spadari, Ciarrocchi and Falaschi, Eur. J. Biochem. 22, 75 (1971)]. The 350-fold purified enzyme gives positive response with four different assays; the rates with the different substrates are different, but the variations are identical to those observed with the purified ligase induced by T4-phage. The enzyme can reconstitute the transforming activity of Bacillus subtilis DNA inactivated by pancreatic DNAase. The human cell enzyme is unable to use a hybrid substrate where an interrupted polydeoxynucleotide is annealed to a polyribonucleotide, whereas in the same conditions the T4 enzyme gives appreciable activity. The partial dependence of the purified enzyme on proteins present in a boiled crude extract, reported in the previous paper, seems due to an aspecific protective effect of the soluble proteins of cell extracts. The enzyme does not show any appreciable sequence specificity in the phosphodiester bond it can form. The purified enzyme can be fractionated into two molecular forms, one having a molecular weight of 190000, the other 95000; fresh extracts of EUE cells contain almost exclusively the high molecular-weight form; ageing of the extract or purification lead to the appearance of the second peak, without variations in the total activity. This could correspond to the conversion of a dimer structure into a monomer. The “dimer” has a pH optimum close to 8.1, whereas the “monomer” has its optimum at 7.5; this explains the bimodal pH curve previously described in the purified enzyme. [ABSTRACT FROM AUTHOR]

The analytical active-enzyme-centrifugation method permits the determination of the hydrodynamic properties of enzymes while they are fully active on their substrates: the centrifugation can be performed at the very dilute concentrations used in kinetic studies (&aysmp; 1 µg/ml): furthermore a purified enzyme preparation is not necessary and in many cases a crude extract is sufficient. This method is beginning to be used in several laboratories even though few of its experimental aspects have been published. This paper reports the details for carrying out, an activeenzyme-centrifugation run, discusses the experimental conditions anti details with artifacts and ways, which are easy, to overcome them. [ABSTRACT FROM AUTHOR]